5bum: Difference between revisions
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<StructureSection load='5bum' size='340' side='right'caption='[[5bum]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='5bum' size='340' side='right'caption='[[5bum]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5bum]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[5bum]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equisetum_arvense Equisetum arvense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BUM FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5bum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bum OCA], [https://pdbe.org/5bum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bum RCSB], [https://www.ebi.ac.uk/pdbsum/5bum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bum ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5bum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bum OCA], [https://pdbe.org/5bum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bum RCSB], [https://www.ebi.ac.uk/pdbsum/5bum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bum ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/C7G3I3_EQUAR C7G3I3_EQUAR] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Equisetum arvense]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fukamizo | [[Category: Fukamizo T]] | ||
[[Category: Kitaoku | [[Category: Kitaoku Y]] | ||
[[Category: Numata | [[Category: Numata T]] | ||
[[Category: Ohnuma | [[Category: Ohnuma T]] | ||
[[Category: Taira | [[Category: Taira T]] | ||
Latest revision as of 19:05, 8 November 2023
Crystal Structure of LysM domain from Equisetum arvense chitinase ACrystal Structure of LysM domain from Equisetum arvense chitinase A
Structural highlights
FunctionPublication Abstract from PubMedA unique GH18 chitinase containing two N-terminal lysin motifs (PrLysM1 and PrLysM2) was first found in fern, Pteris ryukyuensis (Onaga and Taira, Glycobiology, 18, 414-423, 2008). This type of LysM-chitinase conjugates is not usually found in plants but in fungi. Here, we produced a similar GH18 chitinase with one N-terminal LysM module (EaLysM) from the fern, Equisetum arvense (EaChiA, Inamine et al., Biosci. Biotechnol. Biochem., 79, 1296-1304, 2015), using an Escherichia coli expression system and characterized for its structure and mechanism of action. The crystal structure of EaLysM exhibited an almost identical fold (betaalphaalphabeta) to that of PrLysM2. From isothermal titration calorimetry and nuclear magnetic resonance, the binding mode and affinities of EaLysM for chitooligosaccharides (GlcNAc)n (3, 4, 5, and 6) were found to be comparable to those of PrLysM2. The LysM module in EaChiA is likely to bind (GlcNAc)n almost independently through CH-pi stacking of a Tyr residue with the pyranose ring. The (GlcNAc)n-binding mode of LysMs in the LysM-chitinase conjugates from fern plants appears to differ from that of plant LysMs acting in chitin- or Nod-signal perception, in which multiple LysMs cooperatively act on (GlcNAc)n. Phylogenetic analysis suggested that LysM-GH18 conjugates of fern plants formed a monophyletic group and had been separated earlier than forming the clade of fungal chitinases with LysMs. Structure, mechanism, and phylogeny of LysM-chitinase conjugates specifically found in fern plants.,Kitaoku Y, Taira T, Numata T, Ohnuma T, Fukamizo T Plant Sci. 2022 Aug;321:111310. doi: 10.1016/j.plantsci.2022.111310. Epub 2022, May 6. PMID:35696910[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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